NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30695411|ref|NP_568694|]
View 

acetoacetyl-CoA thiolase 2 [Arabidopsis thaliana]

Protein Classification

acetyl-CoA C-acyltransferase( domain architecture ID 11477019)

acetyl-CoA C-acyltransferase catalyzes the formation of acetoacetyl-CoA from acetyl-CoA

EC:  2.3.1.9
Gene Ontology:  GO:0046872|GO:0003985|GO:0006635

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
11-403 0e+00

acetyl-CoA C-acetyltransferase


:

Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 749.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:PLN02644   1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCA 170
Cdd:PLN02644  81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGG 250
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  251 TVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAF 330
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  331 AVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL 403
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
 
Name Accession Description Interval E-value
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
11-403 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 749.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:PLN02644   1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCA 170
Cdd:PLN02644  81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGG 250
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  251 TVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAF 330
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  331 AVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL 403
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
15-383 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 508.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVN 94
Cdd:cd00751   2 IVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTVN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  95 KVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLvDGMLKDGLWDVYNDCGMGSCAELCA 174
Cdd:cd00751  82 RVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 175 EKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGLGK-FDAAKLRKLRPSFKENGgTVT 253
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKG--PVVVDRDEGPRPdTTLEKLAKLKPAFKKDG-TVT 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 254 AGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVV 333
Cdd:cd00751 238 AGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQ 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 30695411 334 ALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:cd00751 318 ALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRY 367
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
11-383 3.82e-180

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 506.53  E-value: 3.82e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFgHDSLVDGMLKDGLWDVYNDCGMGSCA 170
Cdd:COG0183  82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGETA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGLGK-FDAAKLRKLRPSFKEnG 249
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG--EVVVDRDEGPRPdTTLEKLAKLKPAFKK-D 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 250 GTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEA 329
Cdd:COG0183 238 GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 30695411 330 FAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:COG0183 318 FAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRY 371
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
15-401 1.20e-147

acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]


Pssm-ID: 273881 [Multi-domain]  Cd Length: 385  Bit Score: 423.95  E-value: 1.20e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVN 94
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    95 KVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGS-RFGHDSLVDGMLKDgLWDVYNDCGMGSCAELC 173
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGvKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   174 AEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGL-GKFDAAKLRKLRPSFKENgGTV 252
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG--PVTVSSDEGIrPNTTLEKLAKLKPAFDPD-GTV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   253 TAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAV 332
Cdd:TIGR01930 237 TAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAA 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695411   333 VALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLE 401
Cdd:TIGR01930 317 QVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
13-273 4.01e-105

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 310.77  E-value: 4.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    13 VCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTT 92
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    93 VNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLA-EARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAE 171
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   172 LCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPstIVDKDEGL-GKFDAAKLRKLRPSFKEnGG 250
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP--TVDKDEGIrPPTTAEPLAKLKPAFDK-EG 237
                         250       260
                  ....*....|....*....|...
gi 30695411   251 TVTAGNASSISDGAAALVLVSGE 273
Cdd:pfam00108 238 TVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
11-403 0e+00

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 749.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:PLN02644   1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCA 170
Cdd:PLN02644  81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGG 250
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKEDGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  251 TVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAF 330
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  331 AVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL 403
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
15-383 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 508.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVN 94
Cdd:cd00751   2 IVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTVN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  95 KVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLvDGMLKDGLWDVYNDCGMGSCAELCA 174
Cdd:cd00751  82 RVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 175 EKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGLGK-FDAAKLRKLRPSFKENGgTVT 253
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKG--PVVVDRDEGPRPdTTLEKLAKLKPAFKKDG-TVT 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 254 AGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVV 333
Cdd:cd00751 238 AGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQ 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 30695411 334 ALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:cd00751 318 ALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRY 367
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
11-383 3.82e-180

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 506.53  E-value: 3.82e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFgHDSLVDGMLKDGLWDVYNDCGMGSCA 170
Cdd:COG0183  82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGETA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGLGK-FDAAKLRKLRPSFKEnG 249
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG--EVVVDRDEGPRPdTTLEKLAKLKPAFKK-D 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 250 GTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEA 329
Cdd:COG0183 238 GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 30695411 330 FAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:COG0183 318 FAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRY 371
PRK05790 PRK05790
putative acyltransferase; Provisional
10-383 1.24e-170

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 482.34  E-value: 1.24e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   10 PRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVI 89
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   90 CTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSC 169
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  170 AELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPsTIVDKDEGLgKFD--AAKLRKLRPSFKE 247
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDP-VVVDTDEHP-RPDttAESLAKLRPAFDK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  248 NgGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEIN 327
Cdd:PRK05790 239 D-GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEIN 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30695411  328 EAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK05790 318 EAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKK 373
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
15-401 1.20e-147

acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]


Pssm-ID: 273881 [Multi-domain]  Cd Length: 385  Bit Score: 423.95  E-value: 1.20e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVN 94
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    95 KVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGS-RFGHDSLVDGMLKDgLWDVYNDCGMGSCAELC 173
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGvKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   174 AEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGL-GKFDAAKLRKLRPSFKENgGTV 252
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG--PVTVSSDEGIrPNTTLEKLAKLKPAFDPD-GTV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   253 TAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAV 332
Cdd:TIGR01930 237 TAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAA 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695411   333 VALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLE 401
Cdd:TIGR01930 317 QVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
15-381 2.82e-141

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 407.95  E-value: 2.82e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVN 94
Cdd:PRK08235   6 IVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETVN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   95 KVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAELCA 174
Cdd:PRK08235  86 KVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEVA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  175 EKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPsTIVDKDEGLGKfDAA--KLRKLRPSFKENgGTV 252
Cdd:PRK08235 166 KELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDP-IVVAKDEAPRK-DTTieKLAKLKPVFDKT-GTI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  253 TAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAV 332
Cdd:PRK08235 243 TAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAA 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 30695411  333 VALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNG 381
Cdd:PRK08235 323 VALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGG 371
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
13-403 1.16e-136

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 396.57  E-value: 1.16e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   13 VCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTT 92
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   93 VNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYnDCG--MGSCA 170
Cdd:PRK06954  89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAY-DKGrlMGTFA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGLGKFDAAKLRKLRPSFKENgG 250
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKG--DTVIDRDEQPFKANPEKIPTLKPAFSKT-G 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  251 TVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAF 330
Cdd:PRK06954 245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  331 AVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL 403
Cdd:PRK06954 325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
11-382 4.36e-117

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 346.49  E-value: 4.36e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:PRK05656   2 QDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCA 170
Cdd:PRK05656  82 MTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENgG 250
Cdd:PRK05656 162 ENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKD-G 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  251 TVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAF 330
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30695411  331 AVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGK 382
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAK 372
PRK09051 PRK09051
beta-ketothiolase BktB;
11-383 3.02e-111

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 331.54  E-value: 3.02e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQA-PARQAALGAGIPNSVI 89
Cdd:PRK09051   3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMyLSRVAAINAGVPQETP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   90 CTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKdGLWDVYNDCGMGSC 169
Cdd:PRK09051  83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMVG-ALHDPFGTIHMGVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  170 AELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGrpSTIVDKDEGL-GKFDAAKLRKLRPSFKEN 248
Cdd:PRK09051 162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKG--EVVFDTDEHVrADTTLEDLAKLKPVFKKE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  249 GGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINE 328
Cdd:PRK09051 240 NGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30695411  329 AFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRY 374
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
11-403 7.18e-107

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 320.03  E-value: 7.18e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:PRK06366   2 KDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYL-AEARKGSR---FGHDSLVDGMLKDGLWDVYNDCGM 166
Cdd:PRK06366  82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEHM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  167 GSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVsggrgrpstiVDKDEGLGKFDAAKLRKLRPSFK 246
Cdd:PRK06366 162 GVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND----------LDRDEGIRKTTMEDLAKLPPAFD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  247 ENgGTVTAGNASSISDGAAALVLVSgEKAL-QLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGlesSQVDYYE 325
Cdd:PRK06366 232 KN-GILTAGNSAQLSDGGSALVMAS-EKAInEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQN---KSIDYYD 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  326 I---NEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLEL 402
Cdd:PRK06366 307 LvehNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLEM 386

                 .
gi 30695411  403 L 403
Cdd:PRK06366 387 V 387
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
13-273 4.01e-105

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 310.77  E-value: 4.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    13 VCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTT 92
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    93 VNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLA-EARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAE 171
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   172 LCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPstIVDKDEGL-GKFDAAKLRKLRPSFKEnGG 250
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP--TVDKDEGIrPPTTAEPLAKLKPAFDK-EG 237
                         250       260
                  ....*....|....*....|...
gi 30695411   251 TVTAGNASSISDGAAALVLVSGE 273
Cdd:pfam00108 238 TVTAGNASPINDGAAAVLLMSES 260
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
10-383 1.56e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 306.91  E-value: 1.56e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   10 PRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVlSANlGQAPA--RQAALGAGIPNS 87
Cdd:PRK06205   1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQG-YPN-GEAPAigRVAALDAGLPVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   88 VICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFG----HDSLVDGMLKDGLWDVYND 163
Cdd:PRK06205  79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGgvqlHDRLARGRETAGGRRFPVP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  164 CGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPsTIVDKDEGL-GKFDAAKLRKLR 242
Cdd:PRK06205 159 GGMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDP-TVVDRDEHPrADTTLESLAKLR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  243 P--SFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQ 320
Cdd:PRK06205 238 PimGKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDD 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695411  321 VDYYEINEAFAVVALANQKLLGIAP---EKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK06205 318 IDLIELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARY 383
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
11-382 1.16e-98

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 299.25  E-value: 1.16e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIC 90
Cdd:PRK06633   3 KPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   91 TTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSnTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCA 170
Cdd:PRK06633  83 YTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS-LGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  171 ELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSggRGRPSTIVDKDEGLGKFDAAK-LRKLRPSFKENG 249
Cdd:PRK06633 162 ENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVT--IKKTTSLFDHDETVRPDTSLEiLSKLRPAFDKNG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  250 gTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEA 329
Cdd:PRK06633 240 -VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30695411  330 FAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGK 382
Cdd:PRK06633 319 FAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAK 371
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
11-383 3.58e-93

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 285.31  E-value: 3.58e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKR-ANVDPALVQEVVFGnvlSANlgQAP------ARQAALGAG 83
Cdd:PRK09050   2 TEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYG---CAN--QAGednrnvARMSALLAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   84 IPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEArkGSRFG-----HDS-----LVDGML 153
Cdd:PRK09050  77 LPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKA--DSAFSrqaeiFDTtigwrFVNPLM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  154 KDglwdVYNDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPsTIVDKDEGL-GK 232
Cdd:PRK09050 155 KA----QYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDP-VVVDRDEHPrPE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  233 FDAAKLRKLRPSFKEnGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIA 312
Cdd:PRK09050 230 TTLEALAKLKPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLA 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  313 HAGLESSQVDYYEINEAFAVVALANQKLLGIA--PEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK09050 309 RLGLTIDQFDVIELNEAFAAQGLAVLRQLGLAddDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRY 381
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
11-403 2.73e-87

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 270.08  E-value: 2.73e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMG-GFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVL-SANLGQAPARQAALGAGIPNSV 88
Cdd:PRK07661   2 REAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   89 ICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKylaearkgsrFGHDSLVDGMLKDGLWDVYndCGMGS 168
Cdd:PRK07661  82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM----------MGHVVRPNPRLVEAAPEYY--MGMGH 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  169 CAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVS----GGRGRPST---IVDKDEGL-GKFDAAKLRK 240
Cdd:PRK07661 150 TAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTlrtvGENNKLQEetiTFSQDEGVrADTTLEILGK 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  241 LRPSFKENGgTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQ 320
Cdd:PRK07661 230 LRPAFNVKG-SVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSD 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  321 VDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVL 400
Cdd:PRK07661 309 IGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVF 388

                 ...
gi 30695411  401 ELL 403
Cdd:PRK07661 389 ELL 391
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
2-380 9.87e-86

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 268.17  E-value: 9.87e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    2 AHTSESVNPRDVCIVGVARTPM-----GGFLgslSSLPATKLGSLaIAAALKRANVDPALVQEVVFGNVLSANLGQA-PA 75
Cdd:PLN02287  37 AYHRTTAFGDDVVIVAAYRTPIckakrGGFK---DTYPDDLLAPV-LKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnEC 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   76 RQAALGAGIPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLaEARKGSRFGHDSlvdgMLKD 155
Cdd:PLN02287 113 RMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAW-EGGVNPRVESFS----QAQD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  156 GLWDvyndcgMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPV-----EVSGGRGRPSTIvDKDEGL 230
Cdd:PLN02287 188 CLLP------MGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkivDPKTGEEKPIVI-SVDDGI 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  231 -GKFDAAKLRKLRPSFKENGGTvTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPK 309
Cdd:PLN02287 261 rPNTTLADLAKLKPVFKKNGTT-TAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPA 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695411  310 AIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRN 380
Cdd:PLN02287 340 AVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRG 410
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
10-383 1.20e-82

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 257.97  E-value: 1.20e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   10 PRDVCIVGVARTPMG---GflGSLSSLPATKLGSLAIAAALKR-ANVDPALVQEVVFGNVlSANLGQA--PARQAALGAG 83
Cdd:PRK08947   1 MEDVVIVDAIRTPMGrskG--GAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCV-QQTLEQGfnIARNAALLAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   84 IPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTP------------KYLAEArkgsrfghdslvDG 151
Cdd:PRK08947  78 IPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPmnhgvdfhpglsKNVAKA------------AG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  152 MlkdglwdvyndcgMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPsTIVDKDEGLg 231
Cdd:PRK08947 146 M-------------MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVL-KLFDYDEVI- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  232 KFDA--AKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPK 309
Cdd:PRK08947 211 RPETtvEALAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQK 290
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695411  310 AIAHAGLESSQVDYYEINEAFAVVALANQK---LLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK08947 291 ALKRAGLSISDIDVFELNEAFAAQSLPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQF 367
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
12-383 2.37e-82

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 257.62  E-value: 2.37e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   12 DVCIVGVARTPMG----GFLGSlsSLPATKLGSlAIAAALKRA-NVDPALVQEVVFGNVL-SANLGQAPARQAALGAGIP 85
Cdd:PRK09052   7 DAYIVAATRTPVGkaprGMFKN--TRPDDLLAH-VLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   86 NSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTP----KYlaeARKGSRFGHDSLVdGMlkdglwdVY 161
Cdd:PRK09052  84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPmmgnKP---SMSPAIFARDENV-GI-------AY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  162 ndcGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEV-------SGGRGRPST-IVDKDEGlGKF 233
Cdd:PRK09052 153 ---GMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEIterfpdlATGEVDVKTrTVDLDEG-PRA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  234 DAA--KLRKLRPSFKeNGGTVTAGNASSISDGAAALVLVSgEKAL-QLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKA 310
Cdd:PRK09052 229 DTSleGLAKLKPVFA-NKGSVTAGNSSQTSDGAGAVILVS-EKALkQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAA 306
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  311 IAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK09052 307 LKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKY 379
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
11-401 6.36e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 248.48  E-value: 6.36e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPMGGFLGS------LSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQA-PARQAALGAG 83
Cdd:PRK06445   2 EDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   84 IPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGS-RFghdsLVDGMLKDglWDVYN 162
Cdd:PRK06445  82 LPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNpKL----LTDPKYIE--YDLTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  163 DCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSggRGRPSTIVDKDEGLGKfDAA--KLRK 240
Cdd:PRK06445 156 GYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVE--VEGKKKVVDVDQSVRP-DTSleKLAK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  241 LRPSFKENGgTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQ 320
Cdd:PRK06445 233 LPPAFKPDG-VITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKD 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  321 VDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVL 400
Cdd:PRK06445 312 IDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVL 391

                 .
gi 30695411  401 E 401
Cdd:PRK06445 392 E 392
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
15-383 2.00e-78

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 246.93  E-value: 2.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVlSANLGQAP--ARQAALGAGIPNSVICTT 92
Cdd:PRK07801   6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCV-DTIGPQAGniARTSWLAAGLPEEVPGVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   93 VNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPkyLAEARK-GSRFGHDSLVDGmlKDGLWDVYNDCGMGS--C 169
Cdd:PRK07801  85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTaGEQLGFTSPFAE--SKGWLHRYGDQEVSQfrG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  170 AELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVsggrgrpstiVDKDEGLGKFDAAKLRKLRPSFKenG 249
Cdd:PRK07801 161 AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG----------VTVDEGPRETSLEKMAGLKPLVE--G 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  250 GTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEA 329
Cdd:PRK07801 229 GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEA 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30695411  330 FAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK07801 309 FAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRY 362
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
20-401 8.56e-78

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 245.84  E-value: 8.56e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   20 RTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSA-----NLgqapARQAALGAGIPNSVICTTVN 94
Cdd:PRK08131  11 RSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAgedsrNV----ARNALLLAGLPVTVPGQTVN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   95 KVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARK-------------GSRFGHDSLVDGmlkdglwdvY 161
Cdd:PRK08131  87 RLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESafsrdakvfdttiGARFPNPKIVAQ---------Y 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  162 NDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEG-LGKFDAAKLRK 240
Cdd:PRK08131 158 GNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKLVAEDEHpRPSSTVEALTK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  241 LRPSFkeNGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQ 320
Cdd:PRK08131 238 LKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  321 VDYYEINEAFAVVALANQKLLGIA--PEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASAL 398
Cdd:PRK08131 316 MDIIEINEAFASQVLGCLKGLGVDfdDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAM 395

                 ...
gi 30695411  399 VLE 401
Cdd:PRK08131 396 VIE 398
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
12-383 3.15e-76

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 241.60  E-value: 3.15e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   12 DVCIVGVARTPMG-GFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGnvlSAN----LGQAPARQAALGAGIPN 86
Cdd:PRK07108   3 EAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMG---CANpegaTGANIARQIALRAGLPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   87 SVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKylaearkgsRFGHDSLVDGMLKDGLWDVYndCGM 166
Cdd:PRK07108  80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQN---------EMNRHMLREGWLVEHKPEIY--WSM 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  167 GSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPST--------IVDKDEGLgKFDAAK- 237
Cdd:PRK07108 149 LQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKATgrlftkevTVSADEGI-RPDTTLe 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  238 -LRKLRPSFKenGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGL 316
Cdd:PRK07108 228 gVSKIRSALP--GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGL 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695411  317 ESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK07108 306 KVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKY 372
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
15-383 4.88e-75

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 238.47  E-value: 4.88e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSAnlGQAP---ARQAALGAGIPNSVICT 91
Cdd:PRK06504   6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQV--GEQAtnvARNAVLASKLPESVPGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   92 TVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAE---ARKGsrFGHdslvdgMLKDGLWDVYNDCG--- 165
Cdd:PRK06504  84 SIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPStlpAKNG--LGH------YKSPGMEERYPGIQfsq 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  166 -MGscAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTiVDKDEGLgKFDA-----AKLR 239
Cdd:PRK06504 156 fTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEM-HTVDEGI-RFDAtlegiAGVK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  240 KLRPsfkenGGTVTAGNASSISDGAAALVLVSgEKAL-QLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLES 318
Cdd:PRK06504 232 LIAE-----GGRLTAATASQICDGASGVMVVN-ERGLkALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKI 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695411  319 SQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK06504 306 DDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRY 370
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
20-383 1.76e-71

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 229.77  E-value: 1.76e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   20 RTPMGGFL--GSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLS-ANLGQAPARQAALGAGIPNSVICTTVNKV 96
Cdd:PRK08242  11 RTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPvGDQGADIARTAVLAAGLPETVPGVQINRF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   97 CASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKylaearkGSrfghdslvDGmlkdGLWDVYNDCGM-------GSC 169
Cdd:PRK08242  91 CASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM-------GS--------DG----GAWAMDPSTNFptyfvpqGIS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  170 AELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRgrpsTIVDKDEGL-GKFDAAKLRKLRPSFKEN 248
Cdd:PRK08242 152 ADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGL----TILDHDEHMrPGTTMESLAKLKPSFAMM 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  249 GGTV--------------------TAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIP 308
Cdd:PRK08242 228 GEMGgfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATR 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695411  309 KAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PRK08242 308 KALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRT 382
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
15-403 3.54e-71

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 229.12  E-value: 3.54e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   15 IVGVARTPMG-GFLGSLSSLPATKLGSLAIAAAL-KRANVDPALVQEVVFGNVLSA-NLGQAPARQAALGAGIPNsVICT 91
Cdd:PRK07851   6 IVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALdKVPALDPTDIDDLMLGCGLPGgEQGFNMARVVAVLLGYDF-LPGT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   92 TVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPK------------YLAEARK--------GSRFGHDSLVDG 151
Cdd:PRK07851  85 TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKgnsdslpdtknpLFAEAQArtaaraegGAEAWHDPREDG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  152 MLKDglwdVYndCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGrgrpsTIVDKDEG-L 230
Cdd:PRK07851 165 LLPD----VY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDG-----TVVSTDDGpR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  231 GKFDAAKLRKLRPSFKENGgTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKA 310
Cdd:PRK07851 234 AGTTYEKVSQLKPVFRPDG-TVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  311 IAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCN 390
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
                        410
                 ....*....|...
gi 30695411  391 GGGGASALVLELL 403
Cdd:PRK07851 393 GGGQGMAMVLERL 405
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
9-382 4.02e-68

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 221.81  E-value: 4.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    9 NPRDVCIVGVARTPmggFL---GSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIP 85
Cdd:PRK08170   1 MARPVYIVDGARTP---FLkarGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   86 NSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTP--------KYLAE------------ARKGSRFGH 145
Cdd:PRK08170  78 EKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPllfsekmvRWLAGwyaaksigqklaALGKLRPSY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  146 DSLVDGMLKdGLWDVYNDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTwEIVPVEVSGGrgrpsTIVD 225
Cdd:PRK08170 158 LAPVIGLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDG-----KFYD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  226 KDEGLgKFD--AAKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAP 303
Cdd:PRK08170 231 HDDGV-RPDssMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGP 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  304 ALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQ----------KLLG-------IAPEKVNVNGGAVSLGHPLGCSGA 366
Cdd:PRK08170 310 VHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLaawadeeycrEQLGldgalgeLDRERLNVDGGAIALGHPVGASGA 389
                        410
                 ....*....|....*.
gi 30695411  367 RILITLLGILKKRNGK 382
Cdd:PRK08170 390 RIVLHLLHALKRRGTK 405
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
15-401 1.13e-67

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 219.21  E-value: 1.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   15 IVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSA-NLGQAPARQAALGAGIPNSVICTTV 93
Cdd:PRK07850   6 IVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAgEQSNNITRTAWLHAGLPYHVGATTI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   94 NKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKylaearkGSRFGHDSlvdGMLKDGLWDVyNDCGMGSCAELC 173
Cdd:PRK07850  86 DCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL-------GANAGPGR---GLPRPDSWDI-DMPNQFEAAERI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  174 AEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVE--VSGGRGRPS---TIVDKDEGLGKFDAAKLRKLRPSFKen 248
Cdd:PRK07850 155 AKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTgetRLVTRDQGLRDTTMEGLAGLKPVLE-- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  249 GGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINE 328
Cdd:PRK07850 233 GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINE 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  329 AFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLE 401
Cdd:PRK07850 313 AFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
9-401 5.61e-61

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 202.91  E-value: 5.61e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    9 NPRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSanLGQAP--ARQAALGAGIPN 86
Cdd:PRK08963   3 QGDRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQ--MPEAPniAREIVLGTGMNV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   87 SVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTP----KYLAEA----RKGSRFGHD-SLVDGM-LKD- 155
Cdd:PRK08963  81 HTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvsKKLARAlvdlNKARTLGQRlKLFSRLrLRDl 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  156 ------------GLwdvyndcGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSggrgrPSTI 223
Cdd:PRK08963 161 lpvppavaeystGL-------RMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVP-----PYKQ 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  224 VDKDEGLGKFDA--AKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEP-EFFT 300
Cdd:PRK08963 229 PLEEDNNIRGDStlEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDML 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  301 TAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQKLLG-----------------IAPEKVNVNGGAVSLGHPLGC 363
Cdd:PRK08963 309 LGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFAserfareklgrsqaigeVDMSKFNVLGGSIAYGHPFAA 388
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 30695411  364 SGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLE 401
Cdd:PRK08963 389 TGARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLE 426
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
15-403 2.25e-58

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 194.21  E-value: 2.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   15 IVGVARTPMGGFLGSLSSLPATKLgslaiAAALKR---ANVDPAlVQEVVFGNVLSAnlGQAPARQAALGAGIPNSVICT 91
Cdd:PRK06690   5 IVEAKRTPIGKKNGMLKDYEVQQL-----AAPLLTflsKGMERE-IDDVILGNVVGP--GGNVARLSALEAGLGLHIPGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   92 TVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPkylaeARKGSRFGHDSLvdgmlkdglwdvyNDCGMGSCAE 171
Cdd:PRK06690  77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSP-----FQNRARFSPETI-------------GDPDMGVAAE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  172 LCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVevsggrgrpSTIVDKDEGLGKFDAAKLRKLRPSFKENGgT 251
Cdd:PRK06690 139 YVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF---------NGLLDESIKKEMNYERIIKRTKPAFLHNG-T 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  252 VTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFA 331
Cdd:PRK06690 209 VTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFA 288
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695411  332 VVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL 403
Cdd:PRK06690 289 SKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
16-382 4.15e-52

nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238422 [Multi-domain]  Cd Length: 393  Bit Score: 178.84  E-value: 4.15e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  16 VGVARTPMGGFLGSLSSL---PATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTT 92
Cdd:cd00826   1 AGAAMTAFGKFGGENGADandLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  93 VNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAearkgsrfghdslvdgmLKDGLWDVYNDCGMGSCael 172
Cdd:cd00826  81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNA-----------------KEKHIDVLINKYGMRAC--- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 173 caekfqitreqQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPStiVDKDEGLGKFDAAKL---RKLRPSFKENg 249
Cdd:cd00826 141 -----------PDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIH--SDADEYIQFGDEASLdeiAKLRPAFDKE- 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 250 GTVTAGNASSISDGAAALVLVS-------GEKALQLGLLVLAKIKGYGDAAQEPEFFT----TAPALAIPKAIAHAGLES 318
Cdd:cd00826 207 DFLTAGNACGLNDGAAAAILMSeaeaqkhGLQSKAREIQALEMITDMASTFEDKKVIKmvggDGPIEAARKALEKAGLGI 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 319 SQVDYYEINEAFAVVALANQKLLGIAPEK------------------VNVNGGAVSLGHPLGCSGARILITLLGILKKRN 380
Cdd:cd00826 287 GDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEA 366

                ..
gi 30695411 381 GK 382
Cdd:cd00826 367 GK 368
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
12-401 1.18e-51

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 178.43  E-value: 1.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   12 DVCIVGVARTPMG-GFLG--SLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNvlSANLGQAPA---RQAALGAGIP 85
Cdd:PRK06025   3 EAYIIDAVRTPRGiGKVGkgALAHLHPQHLAATVLKALAERNGLNTADVDDIIWST--SSQRGKQGGdlgRMAALDAGYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   86 NSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPkylAEARKGSRFGHDSLVDGMLKDGLWDVYNDCG 165
Cdd:PRK06025  81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTA---AMAAEDMAAGKPPLGMGSGNLRLRALHPQSH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  166 MGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGrgrpSTIVDKDE-GLGKFDAAKLRKLRPS 244
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDG----SVALDHEEfPRPQTTAEGLAALKPA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  245 FK-------ENGGTV------------------TAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFF 299
Cdd:PRK06025 234 FTaiadyplDDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLM 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  300 TTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKR 379
Cdd:PRK06025 314 LNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERR 393
                        410       420
                 ....*....|....*....|..
gi 30695411  380 NGKYGVGGVCNGGGGASALVLE 401
Cdd:PRK06025 394 GLKRGLVTMCAAGGMAPAIIIE 415
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
280-401 1.15e-44

Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 397094 [Multi-domain]  Cd Length: 123  Bit Score: 150.87  E-value: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   280 LLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGH 359
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 30695411   360 PLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLE 401
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
9-381 1.87e-39

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 145.81  E-value: 1.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411    9 NPRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSA----NLgqapARQAALGAGI 84
Cdd:PRK09268   5 TVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHsrdfNL----TRECVLGSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   85 PNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTP--------KYLAEARKGSRFGHD-----SLVDG 151
Cdd:PRK09268  81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrKILLELNRAKTTGDRlkalgKLRPK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  152 MLK----------DGLwdvyndcGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVevsggRGrps 221
Cdd:PRK09268 161 HLApeiprngeprTGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-----LG--- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  222 tiVDKDEGL-GKFDAAKLRKLRPSF-KENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQE---- 295
Cdd:PRK09268 226 --LTRDNNLrPDSSLEKLAKLKPVFgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhg 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  296 PEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQK-----------------LLGIAPEKVNVNGGAVSLG 358
Cdd:PRK09268 304 KEGLLMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycrerlgldapLGSIDRSKLNVNGSSLAAG 383
                        410       420
                 ....*....|....*....|...
gi 30695411  359 HPLGCSGARILITLLGILKKRNG 381
Cdd:PRK09268 384 HPFAATGGRIVATLAKLLAEKGS 406
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
16-372 1.69e-23

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 100.80  E-value: 1.69e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  16 VGVARTPmggfLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVIcTTVNK 95
Cdd:cd00829   1 VGVGMTP----FGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPA-TRVEA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  96 VCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPK-YLAEARKGSRFGHDslvdgmlkdglWDVYNDCGMGSCAELCA 174
Cdd:cd00829  76 AGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTgDEAGGRASDLEWEG-----------PEPPGGLTPPALYALAA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 175 ----EKFQITREQQDDYAVQSFERGIA---AQeagaFTWEIVPVEVSGGRGrpstIVDKdegLGKFDAaklrklrpsfke 247
Cdd:cd00829 145 rrymHRYGTTREDLAKVAVKNHRNAARnpyAQ----FRKPITVEDVLNSRM----IADP---LRLLDC------------ 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 248 nggtvtagnaSSISDGAAALVLVSGEKALQLGLlVLAKIKGYGDAA-----QEPEFFTTAPA--LAIPKAIAHAGLESSQ 320
Cdd:cd00829 202 ----------CPVSDGAAAVVLASEERARELTD-RPVWILGVGAASdtpslSERDDFLSLDAarLAARRAYKMAGITPDD 270
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 321 VDYYEINEAFAVVALANQKLLGIAPE------------------KVNVNGGAVSLGHPLGCSGARILITL 372
Cdd:cd00829 271 IDVAELYDCFTIAELLALEDLGFCEKgeggklvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEA 340
PRK06064 PRK06064
thiolase domain-containing protein;
11-367 1.32e-14

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 74.55  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPmggfLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLS------ANLGQAPARQAALgAGI 84
Cdd:PRK06064   2 RDVAIIGVGQTK----FGELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAglfvsqEHIAALIADYAGL-API 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   85 PnsviCTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAE---ARKGSRFghdslvdgmlkdglWDVY 161
Cdd:PRK06064  77 P----ATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATeaiARAGDYE--------------WEEF 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  162 NDCGMGSCAELCAE----KFQITREQQDDYAVQSFERGIA---AQeagaFTWEIVPVEVSGgrgrpSTIVdkdeglgkfd 234
Cdd:PRK06064 139 FGATFPGLYALIARrymhKYGTTEEDLALVAVKNHYNGSKnpyAQ----FQKEITVEQVLN-----SPPV---------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  235 AAKLRKLrpsfkenggtvtagNASSISDGAAALVLVSGEKALQLGLLVLaKIKGYGDAA-----QEPEFFTT--APALAI 307
Cdd:PRK06064 200 ADPLKLL--------------DCSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQASdtialHDRKDFTTldAAVVAA 264
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695411  308 PKAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIApEK-------------------VNVNGGAVSLGHPLGCSGAR 367
Cdd:PRK06064 265 EKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFA-KKgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVS 342
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
254-382 2.39e-14

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 72.48  E-value: 2.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 254 AGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYG----DAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEA 329
Cdd:cd00327  94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAatfdGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30695411 330 FAVVALANQKLLGIAPEKV---NVNGGAVSLGHPLGCSGARILITLLGILKKRNGK 382
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIP 229
PRK12578 PRK12578
thiolase domain-containing protein;
11-382 5.12e-11

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 63.71  E-value: 5.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPmggfLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVfgnvlsanLGQAPARQAALGAGIPNSVIC 90
Cdd:PRK12578   1 RRVAVIGVGNSK----FGRRDDVSVQELAWESIKEALNDAGVSQTDIELVV--------VGSTAYRGIELYPAPIVAEYS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   91 TTVNKV-------CASGMKAVMIAAQSIQLGINDVVVAGGMESMS--NTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVY 161
Cdd:PRK12578  69 GLTGKVplrveamCATGLAASLTAYTAVASGLVDMAIAVGVDKMTevDTSTSLAIGGRGGNYQWEYHFYGTTFPTYYALY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  162 NDCGMGscaelcaeKFQITREQQDDYAVQSFERGiAAQEAGAFTWEIVPVEVSGGR--GRPSTIVDkdeglgkfdaaklr 239
Cdd:PRK12578 149 ATRHMA--------VYGTTEEQMALVSVKAHKYG-AMNPKAHFQKPVTVEEVLKSRaiSWPIKLLD-------------- 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  240 klrpsfkenggtvtagnASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDA------AQEPEFFT-TAPALAIPKAIA 312
Cdd:PRK12578 206 -----------------SCPISDGSATAIFASEEKVKELKIDSPVWITGIGYAndyayvARRGEWVGfKATQLAARQAYN 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  313 HAGLESSQVDYYEINEAFAVVALANQKLLGIAPE----------------KVNVN--GGAVSLGHPLGCSGARILITLLG 374
Cdd:PRK12578 269 MAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKgkggkfieegqsekggKVGVNlfGGLKAKGHPLGATGLSMIYEITK 348

                 ....*...
gi 30695411  375 ILKKRNGK 382
Cdd:PRK12578 349 QLRDEAGK 356
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
73-366 4.39e-09

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 57.93  E-value: 4.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  73 APARQAALGAGI--PNSVICTTvnkvCASGMKAVMIAAQSIQLGINDVVVAGGMESMSnTPKYLAearkgsrfGHDSlvd 150
Cdd:cd00834 139 MAAGQVAIRLGLrgPNYTVSTA----CASGAHAIGDAARLIRLGRADVVIAGGAEALI-TPLTLA--------GFAA--- 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 151 gmlkdglwdvyndcgMGScaeLCAEkfqitreqQDDYAVQSfergiaaqeagaftweivpvevsggrgRPstivdkdegl 230
Cdd:cd00834 203 ---------------LRA---LSTR--------NDDPEKAS---------------------------RP---------- 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 231 gkFDaaklrklrpsfKENGGTVtagnassISDGAAALVLVSGEKALQLGLLVLAKIKGYG---DAAQEpefftTAP---- 303
Cdd:cd00834 220 --FD-----------KDRDGFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGassDAYHI-----TAPdpdg 274
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695411 304 ---ALAIPKAIAHAGLESSQVDYyeIN------------EAFAVvalanQKLLGIAPEKVNVNGGAVSLGHPLGCSGA 366
Cdd:cd00834 275 egaARAMRAALADAGLSPEDIDY--INahgtstplndaaESKAI-----KRVFGEHAKKVPVSSTKSMTGHLLGAAGA 345
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
258-369 1.48e-08

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 56.19  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  258 SSISDGAAALVLVSGEKALQLGLLVLAKIK------GYGDAAQEPEF-FTTAPALAIP--KAIAHAGLES--SQVDYYEI 326
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKalqlavSNGWELQYNGWdGSYFPTTRIAarKAYREAGITDprEELSMAEV 293
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695411  327 NEAFAVVALANQKLLGIAPE------------------KVNVNGGAVSLGHPLGCSGARIL 369
Cdd:PRK06157 294 HDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
PRK08256 PRK08256
lipid-transfer protein; Provisional
11-127 1.97e-08

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 55.67  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   11 RDVCIVGVARTPmggFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLsanlGQAPARQAAL---G-AGIPn 86
Cdd:PRK08256   1 NKVFVAGVGMTP---FEKPGASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVY----GDSTSGQRALyevGmTGIP- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 30695411   87 sVIctTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESM 127
Cdd:PRK08256  73 -IV--NVNNNCSTGSTALFLARQAVRSGAADCALALGFEQM 110
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
42-370 3.12e-08

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 55.08  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   42 AIAAALKRANVDPALVQEVVFGNVLsanlGQAPARQAALGA----------GIPNSvictTVNKVCASGMKAVMIAAQSI 111
Cdd:PRK06289  33 VVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHLGAmpatvhpalwGVPAS----RHEAACASGSVATLAAMADL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  112 QLGINDVVVAGGMESMSNTPKYLAEARKGSR--FGHDslvdGMLKDGLWDVYndcgMGSCAELCAEKFQITREQQDDYAV 189
Cdd:PRK06289 105 RAGRYDVALVVGVELMKTVPGDVAAEHLGAAawTGHE----GQDARFPWPSM----FARVADEYDRRYGLDEEHLRAIAE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  190 QSFERGIAAQEAGAFTWEIvpvevsggrgrPSTIVDKDEGLGKFDAAKLRKLrpsfkenggtvtagNASSISDGAAALVL 269
Cdd:PRK06289 177 INFANARRNPNAQTRGWAF-----------PDEATNDDDATNPVVEGRLRRQ--------------DCSQVTDGGAGVVL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  270 VSGEKALQL-GLLVLAKIKGYG-------------DAAQEPEFFttaPAL--AIPKAIAHAGLESSQVDYYEINEAFAVV 333
Cdd:PRK06289 232 ASDAYLRDYaDARPIPRIKGWGhrtaplgleqkldRSAGDPYVL---PHVrqAVLDAYRRAGVGLDDLDGFEVHDCFTPS 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30695411  334 ALANQKLLGIAPE------------------KVNVNGGAVSLGHPLGCSGARILI 370
Cdd:PRK06289 309 EYLAIDHIGLTGPgeswkaiengeiaiggrlPINPSGGLIGGGHPVGASGVRMLL 363
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
42-383 1.71e-07

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 52.97  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   42 AIAAALKRANVD--PALVQEVVFGNVLSANLGQ----APARQAALGAGIPNSVI----CTTVNKVCASGMKAVMIAAQSI 111
Cdd:PTZ00455  55 AIQGTLENTGLDgkAALVDKVVVGNFLGELFSSqghlGPAAVGSLGQSGASNALlykpAMRVEGACASGGLAVQSAWEAL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  112 QLGINDVVVAGGMESMSNTpkylaearkGSRFGHDSLVDgmlkdglwdvyndcgmgscaelcAEKFQITReQQDDYAVQS 191
Cdd:PTZ00455 135 LAGTSDIALVVGVEVQTTV---------SARVGGDYLAR-----------------------AADYRRQR-KLDDFTFPC 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  192 F--ERGIAAQEAGAFTWE----IVPVEVSGGRGRP-----STIVDKDEGLGKFDAAKLRKLRPSFKEnggTVTAGNASSI 260
Cdd:PTZ00455 182 LfaKRMKYIQEHGHFTMEdtarVAAKAYANGNKNPlahmhTRKLSLEFCTGASDKNPKFLGNETYKP---FLRMTDCSQV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  261 SDGAAALVLVSGEKALQLGL----LVLAKIKG--------YGDAAQEPEFFTTAPALAipKAIAHAGLESSQVDYYEINE 328
Cdd:PTZ00455 259 SDGGAGLVLASEEGLQKMGLspndSRLVEIKSlacasgnlYEDPPDATRMFTSRAAAQ--KALSMAGVKPSDLQVAEVHD 336
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695411  329 AFAVVALANQKLLGIAPE------------------KVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKY 383
Cdd:PTZ00455 337 CFTIAELLMYEALGIAEYghakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEY 409
PRK07516 PRK07516
thiolase domain-containing protein;
12-365 3.44e-07

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 51.87  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   12 DVCIVGVARTPMGgflgslsSLPATKLGSL---AIAAALKRANVDPALVQEVVFGNVLSANLGQA-PARQAALGAGIPNS 87
Cdd:PRK07516   3 TASIVGWAHTPFG-------KLDAETLESLivrVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDfPASLVLQADPALRF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   88 VICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPkylaearkGSRFGHDSLVDGMLKDGlwdvyNDCGMG 167
Cdd:PRK07516  76 KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP--------TAEVGDILLGASYLKEE-----GDTPGG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  168 SC---AELCAEKFQITREQQDDY---AVQSFERGIA---AQEAGAFTWEIVpvevsggrgrpSTIVDKDeglgKFDAAKL 238
Cdd:PRK07516 143 FAgvfGRIAQAYFQRYGDQSDALamiAAKNHANGVAnpyAQMRKDLGFEFC-----------RTVSEKN----PLVAGPL 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  239 RKLrpsfkenggtvtagNASSISDGAAALVLVSGEKALQLGLLVlakikGYGDAAQEPEFFT---------TAPALAIPK 309
Cdd:PRK07516 208 RRT--------------DCSLVSDGAAALVLADAETARALQRAV-----RFRARAHVNDFLPlsrrdplafEGPRRAWQR 268
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695411  310 AIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPE------------------KVNVNGGAVSLGHPLGCSG 365
Cdd:PRK07516 269 ALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATG 342
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
260-366 2.62e-06

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 49.32  E-value: 2.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 260 ISDGAAALVLVSGEKALQLGLLVLAKIKGYG---DA----AQEPEffTTAPALAIPKAIAHAGLESSQVDYyeIN----- 327
Cdd:COG0304 229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYGassDAyhitAPAPD--GEGAARAMRAALKDAGLSPEDIDY--INahgts 304
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 30695411 328 -------EAFAVvalanQKLLGIAPEKVNVNggavSL----GHPLGCSGA 366
Cdd:COG0304 305 tplgdaaETKAI-----KRVFGDHAYKVPVS----STksmtGHLLGAAGA 345
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
262-366 3.09e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 48.89  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  262 DGAAALVLVSGEKALQLGLLVLAKIKGYG---DA--AQEPEFFTTAPALAIPKAIAHAGLESSQVDYY-------EINEA 329
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGltcDAyhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30695411  330 FAVVALANqkllgIAPEKVNVNGGAVSLGHPLGCSGA 366
Cdd:PRK05952 290 REANLIQA-----LFPHRVAVSSTKGATGHTLGASGA 321
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
262-366 3.28e-06

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 49.02  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  262 DGAAALVLVSGEKALQLGLLVLAKIKGYG---DAaqepeFFTTAP-------ALAIPKAIAHAGLESSQVDYyeIN---- 327
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGmtgDA-----YHMTAPapdgegaARAMKLALKDAGINPEDIDY--INahgt 304
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30695411  328 --------EAFAVvalanQKLLGIAPEKVNVNGGAVSLGHPLGCSGA 366
Cdd:PRK07314 305 stpagdkaETQAI-----KRVFGEHAYKVAVSSTKSMTGHLLGAAGA 346
PRK06158 PRK06158
thiolase; Provisional
260-360 4.79e-06

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 48.10  E-value: 4.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  260 ISDGAAALVLVSGEKALQLG-----LLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVA 334
Cdd:PRK06158 208 VTDGAGAVVMVRADRARDLPrppvyVLGAAAATWHRQISSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINT 287
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 30695411  335 LANQKLLG---------------IAPE---KVNVNGGAVSLGHP 360
Cdd:PRK06158 288 ILFLEDLGfcakgeggafveggrIAPGgrlPVNTNGGGLSCVHP 331
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
263-323 2.02e-04

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 43.10  E-value: 2.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695411  263 GAAALVLVSGEKALQLGLLVLAKIKGYG---DAAQEPEFFTTAPALAIPKAIAHAGLESSQVDY 323
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSmrlDANRGPDPSLEGEMRVIRAALRRAGLGPEDIDY 303
PRK06059 PRK06059
lipid-transfer protein; Provisional
10-132 3.18e-04

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 42.44  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   10 PRDVCIVGVARTPMGGFlgslsSLPATKLGSLAIAAALKRANVDPALVQEVV---------FGNVLSANLGQAPARQaal 80
Cdd:PRK06059   3 PEPVYILGAGMHPWGKW-----GRDFVEYGVVAARAALADAGLDWRDVQLVVgadtirngyPGFVAGATFAQALGWN--- 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30695411   81 gaGIPnsviCTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESmsnTPK 132
Cdd:PRK06059  75 --GAP----VSSSYAACASGSQALQSARAQILAGLCDVALVVGADT---TPK 117
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
260-327 3.53e-04

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 42.31  E-value: 3.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695411  260 ISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQepEFFTT------APAL-AIPKAIAHAGLESSQVDYyeIN 327
Cdd:PRK06501 243 MAEGAGALVLESLESAVARGAKILGIVAGCGEKAD--SFHRTrsspdgSPAIgAIRAALADAGLTPEQIDY--IN 313
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
242-366 3.37e-03

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 39.29  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  242 RPSFKENGGTVtagnassISDGAAALVLVSGEKALQLGLLVLAKIKGYG---DAaqepeFFTTAPA-------LAIPKAI 311
Cdd:PTZ00050 226 RPFDKDRAGFV-------MGEGAGILVLEELEHALRRGAKIYAEIRGYGsssDA-----HHITAPHpdgrgarRCMENAL 293
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695411  312 AHAG-LESSQVDYyeINeAFAVVALANQKLLGIAPEKVNVNGGA----VS-----LGHPLGCSGA 366
Cdd:PTZ00050 294 KDGAnININDVDY--VN-AHATSTPIGDKIELKAIKKVFGDSGApklyVSstkggLGHLLGAAGA 355
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
31-128 3.79e-03

3-oxoacyl-acyl-carrier-protein synthase 3; Provisional


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 39.16  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411   31 SSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANL-GQAPARQAALGAGIPNSVICTTVnkvCASGMKAVMIAAQ 109
Cdd:CHL00203  47 SSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTPDDLfGSASQLQAEIGATRAVAFDITAA---CSGFILALVTATQ 123
                         90
                 ....*....|....*....
gi 30695411  110 SIQLGINDVVVAGGMESMS 128
Cdd:CHL00203 124 FIQNGSYKNILVVGADTLS 142
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
260-323 4.87e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 38.82  E-value: 4.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695411  260 ISDGAAALVLVSGEKALQLGLLVLAKIKGYG---DAAQepeffTTAP-----ALAIPKAIAHAGLESSQVDY 323
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAEIVGFGtnsDGAH-----VTQPqaetmQIAMELALKDAGLAPEDIGY 297
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
260-377 5.19e-03

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 38.77  E-value: 5.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411 260 ISDGAAALVLVSGEKALQLGLLVLAKIKGY-----GDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEIN-----EA 329
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTaatidGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHgtgtpIG 238
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30695411 330 FAVVALANQKLLGiaPEKVNVNGGAVSLGHPLGCSGARILITLLGILK 377
Cdd:cd00825 239 DVKELKLLRSEFG--DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
262-365 5.39e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 38.83  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  262 DGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQepEFFTTAP-------ALAIPKAIAHAGLESSQVDYyeINeAFAVVA 334
Cdd:PRK06333 244 EGAGILVIETLEHALARGAPPLAELVGYGTSAD--AYHMTAGpedgegaRRAMLIALRQAGIPPEEVQH--LN-AHATST 318
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 30695411  335 --------LANQKLLGiAPEKVNVNGGAVSLGHPLGCSG 365
Cdd:PRK06333 319 pvgdlgevAAIKKVFG-HVSGLAVSSTKSATGHLLGAAG 356
PRK08142 PRK08142
thiolase domain-containing protein;
260-342 5.99e-03

thiolase domain-containing protein;


Pssm-ID: 236164 [Multi-domain]  Cd Length: 388  Bit Score: 38.53  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695411  260 ISDGAAALVLVSGEKALQLGLlVLAKIKGYGDAAQEP-----EFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVA 334
Cdd:PRK08142 210 VTDGGGALVVVRPEIARSLKR-PLVKVLGAGEAIKGQmggkvDLTYSGAAWSGPAAFAEAGVTPADIKYASIYDSFTITV 288

                 ....*...
gi 30695411  335 LANQKLLG 342
Cdd:PRK08142 289 LMQLEDLG 296
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH